%0 Journal Article
%@ 1861-471X
%A Venugopalan, Paloth
%A Kishore, Raghuvansh
%D 2015
%F open:1632
%I Wiley
%J Chemistry: an Asian journal
%K X-ray diffraction; foldamers; peptide design; self-association; weak interactions; β-strand mimics
%T Antiparallel Self-Association of a γ,α-Hybrid Peptide: More Relevance of Weak Interactions.
%U http://crdd.osdd.net/open/1632/
%X To learn how a preorganized peptide-based molecular template, together with diverse weak non-covalent interactions, leads to an effective self-association, we investigated the conformational characteristics of a simple γ,α-hybrid model peptide, Boc-γ-Abz-Gly-OMe. The single-crystal X-ray diffraction analysis revealed the existence of a fully extended β-strand-like structure stabilized by two non-conventional C-H⋅⋅⋅O=C intramolecular H-bonds. The 2D (1) H NMR ROESY experiment led us to propose that the flat topology of the urethane-γ-Abz-amide moiety is predominantly preserved in a non-polar environment. The self-association of the energetically more favorable antiparallel β-strand-mimic in solid-state engenders an unusual 'flight of stairs' fabricated through face-to-face and edge-to-edge Ar⋅⋅⋅Ar interactions. In conjunction with FT-IR spectroscopic analysis in chloroform, we highlight that conformationally semi-rigid γ-Abz foldamer in appositely designed peptides may encourage unusual β-strand or β-sheet-like self-association and supramolecular organization stabilized via weak attractive forces.
%Z Copyright of this article belongs to Wiley.